CAZyme Information: POW11289.1

Basic Information

• Species: Puccinia striiformis
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
• CAZyme ID: POW11289.1
• CAZy Family: GH26
• CAZyme Description: Alpha-amylase [Source:UniProtKB/TrEMBL;Acc:A0A2S4VP85]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
573		63958.40	6.9825

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pstriiformis93TX-2	14629	N/A	0	14629

• Gene Location: location=PKSM01000112:107550-110651(+)

Full Sequence      

MGSVYLFFGFIAAWLCLQSTPEIESMHKLSWAFLLGLSTLGLSAKPPSSLRTIATFPLVG
IKNWLVNWRSNRLSQNEQLASCATRHLDDNPPPTGRVTVQLFQWRYSDVGNECEAFLGPN
GYRYVQISPPHEHIEGPQWWTDYQPVSYRIGSKRGSEAEFDAMVQRCASAGVGVIVDVVF
NHMSAGSITEARRGSAGSSYRKYEYSDASLHPFLYSLSSTLTFPPFLTVVSGAISRSATT
WTGTSEQSENQSLRTKRHQTYGWVQNCELVGLADLKTSQRHVQNQLRRYLARLVEKGVTG
LRVDAAKHIPVRDLLDILRFVPLRVVQEIMYTGGEPIRPEEYSTVGRVHIFQAAYDLKRM
FLSDGIAYLGHPVPWGPQWGDGYLPSSQSQIFVTNWDLERNEHSIRIDQHAGPYLLCQVF
ILTWGYGQVDVFSGFNFTAYDEAPQDPVAQCGRFGWRCEHRHPMIIGAIQLGAAASDEPV
QNIVTSGAHRLAFSRGSKVFVAINNDDSDWLLEDVVVGLPLPASPGDAYRDRLHPSGDGQ
LVHLQSDPSCGLTRLRPLSIPPRSAIGIMVFEQ

Enzyme Prediction     

EC	3.2.1.1:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	121	424	2e-68	0.9925650557620818

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	9.49e-112	97	470	3	324	Alpha amylase catalytic domain found in bacterial and eukaryotic Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
200454	AmyAc_bac1_AmyA	4.27e-35	97	375	3	263	Alpha amylase catalytic domain found in bacterial Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
214758	Aamy	1.76e-24	97	186	2	98	Alpha-amylase domain.
200458	AmyAc_euk_AmyA	1.19e-11	125	310	60	212	Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
200451	AmyAc_family	1.12e-09	121	182	38	100	Alpha amylase catalytic domain family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; and C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost this catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDI71468.1|GH13_32	2.42e-98	90	542	27	439
AAA96317.1|GH13_32|3.2.1.1	4.11e-97	90	508	30	409
ADB89947.1|GH13_32	4.11e-97	90	506	30	407
QOV46298.1|GH13_32	8.39e-97	90	542	31	443
BBA97871.1|GH13_32	1.22e-96	91	506	31	409

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1JD9_A	4.40e-73	99	552	6	431	Chain A, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1G94_A	5.40e-73	99	552	6	431	CRYSTAL STRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]
1AQH_A	6.17e-73	99	552	6	431	ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis],1AQM_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS COMPLEXED WITH TRIS [Pseudoalteromonas haloplanktis],1B0I_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis]
1JD7_A	8.64e-73	99	552	6	431	Chain A, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1KXH_A	2.92e-72	99	552	6	431	Chain A, alpha-amylase [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P27350|AMY_STRTL	8.03e-97	90	508	30	409	Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy PE=3 SV=2
sp|P09794|AMY_STRLM	1.70e-90	91	531	30	425	Alpha-amylase OS=Streptomyces limosus OX=1947 GN=aml PE=3 SV=1
sp|P30270|AMY_STRGR	6.60e-90	91	531	30	425	Alpha-amylase OS=Streptomyces griseus OX=1911 GN=amy PE=3 SV=1
sp|P22998|AMY_STRVL	6.61e-81	91	508	30	408	Alpha-amylase OS=Streptomyces violaceus OX=1936 GN=aml PE=2 SV=1
sp|P29957|AMY_PSEHA	4.34e-70	99	552	30	455	Alpha-amylase OS=Pseudoalteromonas haloplanktis OX=228 GN=amy PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.849061	0.150957

TMHMM  Annotations     

There is no transmembrane helices in POW11289.1.